UniProt Accession

 IF5A1_HUMAN; P63241; A8K9A0; D3DTP2; P10159; Q16182; Q7L7L3; Q7Z4L1; Q9D0G2 

Genbank Protein ID

 M23419; S72024; U17969; AY129319; AY129320; AY129321; AY129322; AK292615; CH471108; CH471108; CH471108; CH471108; BC000751; BC001832; BC030160; BC080196; BC085015; BC107779 

Genbank Nucleotide ID

 AAA58453.1; AAD14095.1; AAA86989.1; AAN17514.1; AAN17515.1; AAN17516.1; AAN17518.1; BAF85304.1; EAW90219.1; EAW90220.1; EAW90221.1; EAW90222.1; AAH00751.1; AAH01832.1; AAH30160.1; AAH80196.1; AAH85015.1; AAI07780.1 

Protein Name

 Eukaryotic translation initiation factor 5A-1 

Protein Synonyms/Alias

 eIF-5A-1; eIF-5A1; Eukaryotic initiation factor 5A isoform 1; eIF-5A; Rev-binding factor; eIF-4D 

Gene Name

 EIF5A 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
27	MQCSALRKNGFVVLK	acetylation	[1]
27	MQCSALRKNGFVVLK	ubiquitination	[2, 3]
34	KNGFVVLKGRPCKIV	ubiquitination	[3]
39	VLKGRPCKIVEMSTS	ubiquitination	[3]
47	IVEMSTSKTGKHGHA	acetylation	[1, 4]
67	GIDIFTGKKYEDICP	ubiquitination	[2, 3, 5]
68	IDIFTGKKYEDICPS	acetylation	[6]
68	IDIFTGKKYEDICPS	ubiquitination	[2, 3, 7]
85	NMDVPNIKRNDFQLI	ubiquitination	[2, 7]
121	LPEGDLGKEIEQKYD	ubiquitination	[2, 3, 5]

Reference

 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] The effect of hypusine modification on the intracellular localization of eIF5A.
 Lee SB, Park JH, Kaevel J, Sramkova M, Weigert R, Park MH.
 Biochem Biophys Res Commun. 2009 Jun 12;383(4):497-502. [PMID: 19379712]
 [5] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [6] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647]
 [7] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865] 

Functional Description

 mRNA-binding protein involved in translation elongation. Has an important function at the level of mRNA turnover, probably acting downstream of decapping. Involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity. With syntenin SDCBP, functions as a regulator of p53/TP53 and p53/TP53-dependent apoptosis. Regulates also TNF- alpha-mediated apoptosis. Mediates effects of polyamines on neuronal process extension and survival. May play an important role in brain development and function, and in skeletal muscle stem cell differentiation. Also described as a cellular cofactor of human T-cell leukemia virus type I (HTLV-1) Rex protein and of human immunodeficiency virus type 1 (HIV-1) Rev protein, essential for mRNA export of retroviral transcripts. 

Sequence Annotation

 REGION 20 90 DOHH-binding.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 47 47 N6-acetyllysine.
 MOD_RES 50 50 Hypusine.  

Keyword

 3D-structure; Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Direct protein sequencing; Elongation factor; Endoplasmic reticulum; Hypusine; Membrane; mRNA transport; Nuclear pore complex; Nucleus; Protein biosynthesis; Protein transport; Reference proteome; RNA-binding; Translocation; Transport. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 154 AA 

Protein Sequence

Gene Ontology

 GO:0005642; C:annulate lamellae; IDA:UniProtKB.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 GO:0005643; C:nuclear pore; IDA:UniProtKB.
 GO:0043022; F:ribosome binding; IEA:InterPro.
 GO:0003746; F:translation elongation factor activity; ISS:UniProtKB.
 GO:0017070; F:U6 snRNA binding; IDA:UniProtKB.
 GO:0006917; P:induction of apoptosis; IDA:UniProtKB.
 GO:0006406; P:mRNA export from nucleus; IMP:UniProtKB.
 GO:0008612; P:peptidyl-lysine modification to hypusine; TAS:Reactome.
 GO:0008284; P:positive regulation of cell proliferation; IGI:UniProtKB.
 GO:0045901; P:positive regulation of translational elongation; ISS:UniProtKB.
 GO:0045905; P:positive regulation of translational termination; IEA:InterPro.
 GO:0043687; P:post-translational protein modification; TAS:Reactome.
 GO:0006611; P:protein export from nucleus; IMP:UniProtKB.
 GO:0006452; P:translational frameshifting; IEA:InterPro. 

Interpro

 IPR005824; KOW.
 IPR012340; NA-bd_OB-fold.
 IPR014722; Rib_L2_dom2.
 IPR019769; Trans_elong_IF5A_hypusine_site.
 IPR001884; Transl_elong_IF5A.
 IPR020189; Transl_elong_IF5A_C.
 IPR008991; Translation_prot_SH3-like. 

Pfam

 PF01287; eIF-5a
 PF00467; KOW 

SMART

  

PROSITE

 PS00302; IF5A_HYPUSINE 

PRINTS